Detail Information for IndEnz0005000010
IED ID IndEnz0005000010
Enzyme Type ID lipase000010
Protein Name Hepatic triacylglycerol lipase
HL
Hepatic lipase
EC 3.1.1.3
Lipase member C
Lysophospholipase
EC 3.1.1.5
Phospholipase A1
EC 3.1.1.32
Gene Name Lipc Hpl
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MGNPLQISIFLVFCIFIQSSACGQGVGTEPFGRSLGATEASKPLKKPETRFLLFQDENDRLGCRLRPQHPETLQECGFNSSQPLIMIIHGWSVDGLLENWIWKIVSALKSRQSQPVNVGLVDWISLAYQHYTIAVQNTRIVGQDVAALLLWLEESAKFSRSKVHLIGYSLGAHVSGFAGSSMDGKNKIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSDLQSIGFQCSDMGSFSQGLCLSCKKGRCNTLGYDIRKDRSGKSKRLFLITRAQSPFKVYHYQFKIQFINQIEKPVEPTFTMSLLGTKEEIKRIPITLGEGITSNKTYSFLITLDKDIGELILLKFKWENSAVWANVWNTVQTIMLWGIEPHHSGLILKTIWVKAGETQQRMTFCPENLDDLQLHPSQEKVFVNCEVKSKRLTESKEQMSQETHAKK
Enzyme Length 510
Uniprot Accession Number P27656
Absorption
Active Site ACT_SITE 169; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 195; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 280; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P11150};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000250|UniProtKB:P11150};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P11150};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P11150};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000250|UniProtKB:P11150}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:38651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75735, ChEBI:CHEBI:75938; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652; Evidence={ECO:0000250|UniProtKB:P07867};
DNA Binding
EC Number 3.1.1.3; 3.1.1.5; 3.1.1.32
Enzyme Function FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (By similarity). Also exhibits lysophospholipase activity (By similarity). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (By similarity). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (By similarity). {ECO:0000250|UniProtKB:P07867, ECO:0000250|UniProtKB:P11150}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Glycosylation (2); Region (1); Sequence conflict (1); Signal peptide (1)
Keywords Glycoprotein;HDL;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11150}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000250|UniProtKB:P11150
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10357838; 10482304; 10744773; 10787427; 11208732; 11290828; 11842132; 11906928; 11971936; 12117557; 12700335; 12897204; 12939599; 12975454; 14610273; 14679168; 14681479; 14974682; 14981222; 15181537; 15205216; 15304509; 15314098; 15520453; 15995171; 16141072; 16368783; 16397139; 16498401; 17071916; 17103052; 17234195; 17431181; 17872590; 18175806; 18599739; 19524061; 19783858; 19965617; 20056822; 20373033; 20558822; 21267068; 21677750; 21730028; 21750705; 22323595; 23328279; 23355893; 23376223; 24440515; 24777581; 24818611; 25209997; 2563260; 25862097; 25875831; 26423094; 27172975; 3109891; 31202927; 34197964; 3470738; 6804942; 7852377; 8105016; 8288233; 8560269; 8672141; 8798380; 8827514; 9153204; 9338114; 9442022; 9616220; 9630674; 9717727; 9861024; 9918035;
Motif
Gene Encoded By
Mass 57,389
Kinetics
Metal Binding
Rhea ID RHEA:12044; RHEA:15177; RHEA:18689; RHEA:38575; RHEA:38576; RHEA:38699; RHEA:38700; RHEA:40475; RHEA:40476; RHEA:41384; RHEA:41385; RHEA:38511; RHEA:38512; RHEA:38391; RHEA:38392; RHEA:40499; RHEA:40500; RHEA:40435; RHEA:40436; RHEA:38651; RHEA:38652
Cross Reference Brenda